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Updated: Apr 8, 2026

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

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Published on: April 9, 2017

Deamidation Promotes AGE-Modifications in Human Lens γS-Crystallin.

Sudipta Panja¹, Ram H Nagaraj¹

¹Department of Ophthalmology, University of Colorado Anschutz, Aurora, Colorado 80045, United States.

|April 7, 2026

Summary

This summary is machine-generated.

Deamidation of eye lens proteins like gamma-S-crystallin promotes advanced glycation end product (AGE) formation. Further oxidation increases susceptibility, contributing to protein aggregation in lens aging and cataracts.

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Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

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Published on: March 7, 2019

Area of Science:

Biochemistry
Ophthalmology
Protein Chemistry

Background:

Deamidation and advanced glycation end products (AGEs) are key post-translational modifications (PTMs) in eye lens proteins.
These PTMs contribute to protein aggregation, light scattering, lens aging, and cataract formation.
The interplay between deamidation and AGE formation remains poorly understood.

Purpose of the Study:

To investigate the relationship between deamidation and AGE formation in gamma-S-crystallin (γSC).
To determine how deamidation affects AGE accumulation and cross-linking in γSC.
To explore the combined effects of deamidation and oxidation on AGE formation in γSC.

Main Methods:

Mimicked deamidation in γSC by mutating asparagine residues to aspartic acid.
Incubated deamidation mimics with a glycating mixture.
Evaluated AGE formation using Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS).
Investigated the impact of oxidation (GSSG) on deamidated γSC.

Main Results:

Deamidation significantly promoted the formation of both non-cross-linking and cross-linking AGEs in lysine residues of γSC.
Deamidated γSC variants (N14D, N143D, triple deamidated) showed higher AGE accumulation than native γSC.
Oxidation of deamidated γSC further increased AGE formation, indicating heightened susceptibility.

Conclusions:

Deamidation acts as a catalyst for AGE formation in γSC.
Oxidation exacerbates AGE modifications in deamidated γSC.
The synergistic effects of deamidation, oxidation, and AGEs likely drive protein cross-linking and aggregation in age-related cataracts.